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Relative Quantitation of Proteins with Isotope Tagged Technique in Mass Spectrometry

2007년 2월 20일 03시 46분 55초
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분석화학 - Advanced Analytical Techniques
저자 및
한국기초과학지원연구원 연구장비개발부,
An initial step in the systematic analysis of biological processes is the measurement of expression level of relevant sets of proteins. The accurate quantification of proteins is the essential goal for exploring cellular functions and processes in proteomics. Recently, quantitative approaches utilizing mass spectrometry with a host of stable-labeling chemistries have emerged. The isotope coded tagging strategy is perhaps the best characterized method for relative protein quantification using mass spectrometry. Other elegant approaches use cell-culture enrichment with a stable isotope labeled amino acid, including arginine, lysine, tyrosine, and leucine, for in vivo incorporation of a mass difference to support relative quantitation. This circumvents potential difficulties surrounding chemical labeling downstream in a comparative experiment. We have applied the stable isotope labeled amino acid method to analyze the different quantities of proteins cultured from neural stem cell. A multiplexed set of reagents has also been developed for quantitative protein analysis that place isobaric mass labels at the N termini and lysine side chains of peptides. For the different proteome analysis of colorectal cancer tissue in comparison to normal one, we have applied the isobaric tagging method in vitro with a set of amine reactive isobaric tags for quantitation.